The article reviews the mutations in the spike protein of SARS-CoV-2, focusing on their impacts on antigenicity and their context within the protein structure. It highlights the emergence of variants with increased transmissibility and antigenic changes, which may affect immune recognition and vaccine effectiveness. Key mutations discussed include D614G, N439K, Y453F, and E484K, which enhance infectivity, reduce neutralizing antibody activity, and increase ACE2 binding affinity. The article also explores the structural context of these mutations, their impact on antibody binding, and their frequency in global sequence datasets. Additionally, it discusses mechanisms of antigenic change, such as amino acid substitutions, increasing receptor-binding avidity, changes in glycosylation, deletions, insertions, and allosteric structural effects. The review emphasizes the need for continued surveillance and research to understand and address the evolving nature of SARS-CoV-2 variants.The article reviews the mutations in the spike protein of SARS-CoV-2, focusing on their impacts on antigenicity and their context within the protein structure. It highlights the emergence of variants with increased transmissibility and antigenic changes, which may affect immune recognition and vaccine effectiveness. Key mutations discussed include D614G, N439K, Y453F, and E484K, which enhance infectivity, reduce neutralizing antibody activity, and increase ACE2 binding affinity. The article also explores the structural context of these mutations, their impact on antibody binding, and their frequency in global sequence datasets. Additionally, it discusses mechanisms of antigenic change, such as amino acid substitutions, increasing receptor-binding avidity, changes in glycosylation, deletions, insertions, and allosteric structural effects. The review emphasizes the need for continued surveillance and research to understand and address the evolving nature of SARS-CoV-2 variants.